Research workbench
CBM35 from cellvibrio japonicus ABF62
Analyse CBM35 from cellvibrio japonicus ABF62 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W46
- Type
- protein
- Length
- 273 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase D
- EC
- 3.2.1.55
- UniProt
- Q51815
- Ligands
- CA, NA
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase D (EC 3.2.1.55) | protein | 138 | 0% helix, 53% strand | Q51815 |
| B | Esterase D (EC 3.2.1.55) | protein | 135 | 0% helix, 53% strand | Q51815 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.49 | 0.78 | 31 | empty |
| 2 | 61 | 0.28 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 356 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2W46 · CBM35 from Cellvibrio japonicus Abf62 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q51815
- Elsewhere: RCSB PDB 2W46 · PDBe 2W46 · UniProt Q51815
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